4.7 Article

Algal Protein Kinase, Triacylglycerol Accumulation Regulator 1, Modulates Cell Viability and Gametogenesis in Carbon/Nitrogen-Imbalanced Conditions

Journal

PLANT AND CELL PHYSIOLOGY
Volume 60, Issue 4, Pages 916-930

Publisher

OXFORD UNIV PRESS
DOI: 10.1093/pcp/pcz010

Keywords

C/N balance; Chlamydomonas; Dual-specificity tyrosine-phosphorylation-regulated kinase; Gametogenesis; Hydrogen peroxide; Phosphoproteome

Funding

  1. Japan Society for the Promotion of Science [25120714, 16H04805, 15K18682, 15H01247]
  2. Advanced Low Carbon Technology Research and Development Program of Japan Science and Technology Agency [JPMJAL1105]
  3. Cooperative Research Grant of the Genome Research for BioResources, NODAI Genome Research Center, Tokyo University of Agriculture
  4. Grants-in-Aid for Scientific Research [15K18682, 16H04805, 15H01247] Funding Source: KAKEN

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Nutrient-deprived microalgae accumulate triacylglycerol (TAG) in lipid droplets. A dual-specificity tyrosine phosphorylation-regulated kinase, TAG accumulation regulator 1 (TAR1) has been shown to be required for acetate-dependent TAG accumulation and the degradation of chlorophyll and photosynthesis-related proteins in photomixotrophic nitrogen (N)-deficient conditions (Kajikawa etal. 2015). However, this previous report only examined particular condition. Here, we report that in photoautotrophic N-deficient conditions, tar1-1 cells, with a mutation in the TAR1 gene, maintained higher levels of cell viability and lower levels of hydrogen peroxide generation and accumulated higher levels of TAG and starch compared with those of wild type (WT) cells with bubbling of air containing 5% carbon dioxide. Transcriptomic analyses suggested that genes involved in the scavenging of reactive oxygen species are not repressed in tar1-1 cells. In contrast, the mating efficiency and mRNA levels of key regulatory genes for gametogenesis, MID, MTD and FUS, were suppressed in tar1-1 cells. Among the TAR1-dependent phosphopeptides deduced by phosphoproteomic analysis, protein kinases and enzymes related to N assimilation and carbon (C) metabolism are of particular interest. Characterization of these putative downstream factors may elucidate the molecular pathway whereby TAR1 mediates cellular propagation and C and N metabolism in C/N-imbalanced stress conditions.

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